Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.
Description
Structure of the bacteriophage phi29 DNA packaging mo... [Nature. 2000] - PubMed - NCBI
%0 Journal Article
%1 motor
%A Simpson, A A
%A Tao, Y
%A Leiman, P G
%A Badasso, M O
%A He, Y
%A Jardine, P J
%A Olson, N H
%A Morais, M C
%A Grimes, S
%A Anderson, D L
%A Baker, T S
%A Rossmann, M G
%D 2000
%J Nature
%K phage
%N 6813
%P 745-750
%R 10.1038/35047129
%T Structure of the bacteriophage phi29 DNA packaging motor
%U http://www.ncbi.nlm.nih.gov/pubmed/11130079
%V 408
%X Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.
@article{motor,
abstract = {Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.},
added-at = {2014-02-22T14:32:21.000+0100},
author = {Simpson, A A and Tao, Y and Leiman, P G and Badasso, M O and He, Y and Jardine, P J and Olson, N H and Morais, M C and Grimes, S and Anderson, D L and Baker, T S and Rossmann, M G},
biburl = {https://www.bibsonomy.org/bibtex/2708ee63b193c02fad61eaa638c5a66cd/ross_mck},
description = {Structure of the bacteriophage phi29 DNA packaging mo... [Nature. 2000] - PubMed - NCBI},
doi = {10.1038/35047129},
interhash = {0eb743b4e2c95bdcca01e455cd7fcbb7},
intrahash = {708ee63b193c02fad61eaa638c5a66cd},
journal = {Nature},
keywords = {phage},
month = dec,
number = 6813,
pages = {745-750},
pmid = {11130079},
timestamp = {2014-02-22T14:32:21.000+0100},
title = {Structure of the bacteriophage phi29 DNA packaging motor},
url = {http://www.ncbi.nlm.nih.gov/pubmed/11130079},
volume = 408,
year = 2000
}